Journal
JOURNAL OF GENERAL VIROLOGY
Volume 92, Issue -, Pages 188-194Publisher
SOC GENERAL MICROBIOLOGY
DOI: 10.1099/vir.0.024984-0
Keywords
-
Categories
Funding
- Ministerio de Educacion y Ciencia, Spain [BFU-2008-03784, BFU-2008-01108/BMC]
- CSIC
- Comunidad de Madrid
- Juan de la Cierva Program
- JAE CSIC
- IFARHU-SENACYT of Panama
Ask authors/readers for more resources
The multifunctional Kaposi's sarcoma-associated herpesvirus (KSHV) latent protein latency-associated nuclear antigen 2 (LANA2) has a critical role in KSHV-induced B-cell malignancies. LANA2 increases the level of small ubiquitin-like modifier (SUMO)2-ubiquitin-modified PML and induces the disruption of PML oncogenic domains (PODs) by a process that requires a non-covalent SUMO interaction domain (SIM) in LANA2. We now demonstrate that LANA2 is covalently conjugated to SUMO1 and SUMO2 both in vitro and in latently KSHV-infected B-cells. We show that a LANA2 SIM mutant exhibits a slightly altered sumoylation pattern, which suggests that non-covalent SUMO interactions represent a mechanism for determining SUMO substrate recognition and modification. In addition, several lysine residues were mapped as SUMO conjugation sites. A sumoylation-deficient mutant shows impaired ability to induce disruption of PODs, which suggests that either directly bound or covalently conjugated SUMO moieties may act as a bridge for interaction between LANA2 and other SUMO-modified or SUMO-interacting proteins required for disruption of PODs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available